recommended for detection of TRIM9 of human origin by WB, IP and ELISA
Modification Notes
The tripartite motif (TRIM) family of proteins are characterized by a conserved TRIM domain that includes a coiled-coil region, a B-box type zinc finger, one RING finger and three zinc-binding domains. TRIM9 (Tripartite motif-containing protein 9), also known as RNF91 (RING finger protein 91), is a 710 amino acid protein that contains a variety of domains that are characteristic to TRIM proteins, including a RING-type zinc finger and two B box-type zinc fingers, as well as a fibronectin type-III domain, a COS domain and a B30.2/SPRY domain. TRIM9 utilizes its coiled coil domain to mediate the interaction with the amino-terminal t-SNARE domain of SNAP25. In this manner, TRIM9 acts as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the formation of the SNARE complex. There are three isoforms of TRIM9 that are produced as a result of alternative splicing events.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPELISA
WB:1:500~1:2000 IP:1:100~1:500 Notes:Optimal dilutions/concentrations should be determined by the researcher.
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
recommended for detection of TRIM9 of human origin by WB IP and ELISA
Tissue Specificity
recommended for detection of TRIM9 of human origin by WB, IP and ELISA